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Description

Albumins are a group of acidic proteins which occur in the body fluids and tissues of mammals and in some plant seeds. Serum and plasma albumin is carbohydrate-free and comprises 55-62% of the protein present. However, only about 40% of the total albumin in the body is in the circulating plasma at one time with the remainder being in extracellular spaces with which there is, in general, equilibration about every 24 hours. Bovine albumin is a single polypeptide chain consisting of approximately 583 to 595 amino acid residues and no carbohydrates. At pH 5-7, it contains 17 intrachain disulfide bridges and 1 sulfhydryl group. E.J. Cohn and associates developed one of the first commercial precipitation procedures using an alcohol precipitation. Additional removal of impurities can be accomplished by crystallization, preparative electrophoresis, ion exchange chromatography, affinity chromatography (e.g., ConA-agarose removes glycoproteins), heat treatment (removes globulins), low pH treatment, charcoal treatment, organic solvent precipitation (i.e. isooctane) and low temperature treatment. Charcoal treatment and organic solvent precipitation remove fatty acids. Albumin binds water, Ca2+, Na+ and K+. Due to a hydrophobic cleft, albumin binds fatty acids, bilirubin, hormones and drugs. The main biological function of albumin is to regulate the colloidal osmotic pressure of blood and to a lesser degree to provide cellular nutrition. Human and bovine albumins contain 16% nitrogen.

Applications

AlbumiNZ™ Low IgG BSA supports growth of stem cells and increases protein production from hybridoma cells. Albumin is also used to solubilize lipids, and as a blocking agent in Western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present such as electrophoresis.

Product Overview

Serum albumin may be referred to as Cohn Fraction V. This naming convention is taken from the original Cohn method of fractionating serum proteins using cold ethanol precipitation. Serum albumin was found in the fifth ethanol fraction using Cohn′s method. Since then, the term "Cohn Fraction V" has been used by some to describe serum albumin regardless of the method of preparation. Others have used this term to describe serum albumin purified by ethanol fractionation methods that have been highly modified since the original Cohn method was described.

Product Description

AlbumiNZ™ Low IgG BSA is chromatographically purified from New Zealand-sourced bovine plasma in an ISO quality system assuring complete traceability and consistent high quality. This albumin has very low endotoxin and low IgG to simplify downstream purification, is tested for the absence of viruses according to 9CFR and has the highest possible biosafety level. The albumin supports growth of stem cells and increases protein production from hybridoma cells.

Biochem/physiol Actions

Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Albumins are readily soluble in water and can only be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of albumin is very good (especially if the solutions are stored aliquoted and frozen). Albumin is readily coagulated by heat. When heated to 50 °C or above, albumin quite rapidly forms hydrophobic aggregates which do not revert to monomers upon cooling.